Mouse Heparanase (HPSE) Protein
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Description
Mouse Heparanase (HPSE) Protein is a recombinant Mouse protein expressed in HEK293 cells.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Host | HEK293 cells |
| Origin | Mouse |
| Observed MW | Molecular Weight: Calculated MW: 58.74 kDa Observed MW (SDS-PAGE): 70 kDa Sequence Fragment: Met1-Ile535 Tag: C-terminal His tag |
| Expression | Recombinant |
| Purity | >95% (SDS-PAGE) |
| Size 1 | 20 µg |
| Size 2 | 100 µg |
| Form | Lyophilized Reconstitute in sterile H2O. Do not vortex. |
| Tested Applications | SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4, containing 5% - 8% Trehalose, Mannitol and 0.01% Tween-80. |
| Availability | Shipped within 5-15 working days. |
| Storage | Store lyophilized between -20 °C and -80 °C. |
| Dry Ice | No |
| UniProt ID | Q6YGZ1 |
| Gene ID | 15442 |
| Background | Protein HPSE |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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Human HPSE (Heparanase) ELISA Kit
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HPSE antibody
Endoglycosidase that cleaves heparan sulfate proteoglycans(HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix(ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extacellular matrix(ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.
Ver ProductoHPSE antibody
Endoglycosidase that cleaves heparan sulfate proteoglycans(HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix(ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extacellular matrix(ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.
Ver Producto